The long-term goal of this research is to understand the structural and energetic consequences to a protein target on binding volatile anesthetic molecules. It offers experimental techniques that compliment those peptides in search of a unitary view of what protein structural characteristics select of anesthetic binding and how the energetics of protein-anesthetic interactions alter thermodynamic stability of the secondary, tertiary, and quaternary structure. The investigators propose to determine binding energetics and effects of volatile anesthetic agents on the folding stability of model homopolymers, four-alpha-helix bundles and model ion channels. Several biologic proteins known to bind inhalational anesthetics, such as bovine serum albumen, adenylate kinease, haloalkane dehalogenase, and the luciferases will also be studied. A principle method of analysis will be differential scanning calorimetry and isothermal titration calorimetry. The investigators also propose to determine the effects of volatile anesthetic agents on folding stability and activity of G proteins. Stability analyses will include non-thermal perturbants such as pH and chaotropic agents (urea, guanidium chloride) together with optical approaches including UV absorbance, tryptophan fluorescence, optical rotation, and infrared methods. Finally, the investigators wish to relate the changes in individual signaling protein stability produced by volatile anesthetics as found by the above physical methods to bimolecular signalling using several spectroscopic and other methods developed in this lab. The visual G protein couple signal transduction system will be used because it is a well define representative of the enormous family of G protein couple receptors.